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Database: UniProt/TrEMBL
Entry: A0A0K0XCK3_9MYCO
LinkDB: A0A0K0XCK3_9MYCO
Original site: A0A0K0XCK3_9MYCO 
ID   A0A0K0XCK3_9MYCO        Unreviewed;       508 AA.
AC   A0A0K0XCK3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   RecName: Full=Probable DNA ligase {ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=ligB {ECO:0000313|EMBL:AKS35133.1};
GN   Synonyms=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   ORFNames=AFA91_28135 {ECO:0000313|EMBL:AKS35133.1};
OS   Mycobacterium goodii.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=134601 {ECO:0000313|EMBL:AKS35133.1};
RN   [1] {ECO:0000313|EMBL:AKS35133.1, ECO:0000313|Proteomes:UP000062255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X7B {ECO:0000313|EMBL:AKS35133.1,
RC   ECO:0000313|Proteomes:UP000062255};
RA   Yu B., Li F., Xu P.;
RT   "Complete genome sequence of Mycobacterium goodii X7B, a facultative
RT   thermophilic biodesulfurizing bacterium.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU000617}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP012150; AKS35133.1; -; Genomic_DNA.
DR   RefSeq; WP_049747591.1; NZ_CP012150.1.
DR   EnsemblBacteria; AKS35133; AKS35133; AFA91_28135.
DR   KEGG; mgo:AFA91_28135; -.
DR   PATRIC; fig|134601.6.peg.5811; -.
DR   KO; K10747; -.
DR   Proteomes; UP000062255; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000062255};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:AKS35133.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617}.
FT   DOMAIN      297    412       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    215    215       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     213    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     220    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     235    235       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     300    300       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     372    372       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     378    378       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   508 AA;  53998 MW;  E84A8441878A5E78 CRC64;
     MLLADVAAAS TEVAASSARL AKIDRIATLL ARAAADGDAQ AVAVTVSWLS GELPQRQIGV
     GWAALRSLPP PAATASLTVD EVDDRFGAIK AVAGKGSQAT RAGLVRDLFG AATEVEQKFL
     RRLLSGELRQ GALTGVMADA VARAADLPAA EIRRAAMLAG NLPAVAAAAV TGGRSALAEF
     RLQVGRPVGP MLAQTATSVA DALERLGGTA VLEAKLDGAR VQIHRHGTEV SVYTRSLDDV
     THRLPEVVEA TLALPATDLI ADAEAIALRP DGRPHPFQVT AARFGRKDPR DLDPLSVFFF
     DLLHIDGRDL LDLSTEERFG ALDALVPPSH RVDRLVTADA DDAQAFLDRT LAAGHEGVMA
     KSPGAPYEAG RRGAGWLKVK PVHTLDLVVL AVEWGSGRRT GKLSNIHLGA RDPLTGEFVM
     LGKTFKGMTD AMLEWQTRRF TDLADGPTDG NVVKVRPEQV VEIAFDGVQR SSRYPGGMAL
     RFARVVRYRD DKTSDEVDTT DTVRAFLG
//
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